Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity.

PLoS genetics - 1 Jan 2013

Cloutier Philippe, Lavallée-Adam Mathieu, Faubert Denis, Blanchette Mathieu, Coulombe Benoit

Abstract excerpt

Methylation is a post-translational modification that can affect numerous features of proteins, notably cellular localization, turnover, activity, and molecular interactions. Recent genome-wide analyses have considerably extended the list of human genes encoding putative methyltransferases. Studies on protein methyltransferases have revealed that the regulatory function of methylation is not limited to...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Frontotemporal Dementia
Share to HSP70 Heat-Shock Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HSP90 Heat-Shock Proteins

Share to Mass Spectrometry

Share to Methylation

Share to Methyltransferases

Share to Myositis, Inclusion Body

Share to Osteitis Deformans

Source

Open in PubMed Open full text

Identifiers

PMID: 23349634
DOI: 10.1371/journal.pgen.1003210
PMCID: PMC3547847

Genes

VCP
ASPSCR1
HSPA8
KIN

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity.PMID 23349634Read ↗

AI-empowered integrative structural characterization of m6A methyltransferase complexSemantic proximity Read ↗

From histones to ribosomes: a chromatin regulator tangoes with translation.Semantic proximity Read ↗

Cofactors-loaded quaternary structure of lysine-specific demethylase 5C (KDM5C) protein: Computational model.Semantic proximity Read ↗

Mapping the MOB proteins’ proximity network reveals a unique interaction between human MOB3C and the RNase P complexSemantic proximity Read ↗

A method for systematic mapping of protein lysine methylation identifies functions for HP1β in DNA damage response.Semantic proximity Read ↗

Post-Translational Variants of Major Proteins in Amyotrophic Lateral Sclerosis Provide New Insights into the Pathophysiology of the Disease.Semantic proximity Read ↗

Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.Semantic proximity Read ↗

Lysine Methyltransferase SMYD1 Regulates Myogenesis via skNAC Methylation.Semantic proximity Read ↗

The methyltransferase METTL9 mediates pervasive 1-methylhistidine modification in mammalian proteomes.Semantic proximity Read ↗

Discerning evolutionary trends in post-translational modification and the effect of intrinsic disorder: Analysis of methylation, acetylation and ubiquitination sites in human proteinsSemantic proximity Read ↗

Class II Histone Deacetylases: from Sequence to Function, Regulation, and Clinical ImplicationSemantic proximity Read ↗

The Interplay of Acetylation and Ubiquitination Controls PRMT1 HomeostasisSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.